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    SUMOylation of SERCA2a

    SUMOylation of SERCA2a

    SUMOylation is essential for preserving the stability and activity of SERCA2a

    Calcium-transporting ATPase ATP2A2, also known as SERCA2a, is a critical ATPase responsible for Ca2+ re-uptake during excitation–contraction (E-C) coupling. Impaired Ca2+ uptake resulting from decreased expression and reduced activity of SERCA2a is a hallmark of heart failure

    Roger Hajjar and co-workers have demonstrated that SUMOylation is essential for preserving the stability and activity of SERCA2a and that levels of SUMO1 are decreased in failing hearts.  They also show in a mouse model of heart failure that gene delivery of SUMO1 can restore heart function to the same degree as delivery of SERCA2a, pointing to SUMO1 as a potential therapeutic candidate for treating heart failure. Read the paper here.

    Key findings to date:

    • SERCA2a is SUMOylated at lysines 480 and 585 
    • SUMOylation is essential for preserving SERCA2a ATPase activity and stability in mouse and human cells
    • Levels of SUMO1 and the SUMOylation of SERCA2a are greatly reduced in failing hearts
    • SUMO1 overexpression in isolated cardiomyocytes augments contractility and accelerates Ca2+ decay
    • SUMOylation is a critical post-translational modification that regulates SERCA2a function 
    • Findings may provide a platform for the design of novel therapeutic strategies for heart failure.

    Which tools do I need? Badrilla is pleased to offer new panel of reagents to facilitate the study of SERCA and SUMOylation in your experimental workflow.

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